L_VSNJH
ID L_VSNJH Reviewed; 2109 AA.
AC P13615;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=RNA-directed RNA polymerase L;
DE Short=Protein L;
DE AltName: Full=Large structural protein;
DE AltName: Full=Replicase;
DE AltName: Full=Transcriptase;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48 {ECO:0000250|UniProtKB:P28887};
DE Includes:
DE RecName: Full=GTP phosphohydrolase {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P03523};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=PRNTase {ECO:0000305};
DE Includes:
DE RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE EC=2.1.1.375 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=G-N7-MTase {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=N1-2'-O-MTase {ECO:0000250|UniProtKB:P03523};
GN Name=L;
OS Vesicular stomatitis New Jersey virus (strain Hazelhurst subtype
OS Hazelhurst) (VSNJV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11281;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2833012; DOI=10.1016/0042-6822(88)90276-0;
RA Feldhaus A.L., Lesnaw J.A.;
RT "Nucleotide sequence of the L gene of vesicular stomatitis virus (New
RT Jersey): identification of conserved domains in the New Jersey and Indiana
RT L proteins.";
RL Virology 163:359-368(1988).
CC -!- FUNCTION: Responsible for RNA synthesis (replicase and transcriptase),
CC cap addition, and cap methylation (By similarity). Performs also the
CC polyadenylation of subgenomic mRNAs by a stuttering mechanism at a
CC slipery stop site present at the end of viral genes (By similarity).
CC The template is composed of the viral RNA tightly encapsidated by the
CC nucleoprotein (N) (By similarity). The viral polymerase binds to the
CC genomic RNA at the 3' leader promoter, thereby initiating either genome
CC replication or mRNA transcription. In the transcription mode, the
CC polymerase performs the sequential transcription of all mRNAs using a
CC termination-reinitiation mechanism responding to gene start and gene
CC end signals. Some polymerase disengage from the template at each gene
CC junction, resulting in a decreasing abundance of transcripts from the
CC 3' to the 5' end of the genome (By similarity). The first gene is the
CC most transcribed, and the last the least transcribed. The viral
CC phosphoprotein helps the polymerase to engage the N-RNA template and
CC acts as processivity factor. Polyribonucleotidyl transferase (PRNTase)
CC adds the cap structure when the nascent RNA chain length has reached
CC few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC facilitates subsequent guanine-N-7 methylation, both activities being
CC carried by the viral polymerase (By similarity). In the replication
CC mode, the polymerase replicates the whole viral genome without
CC recognizing the gene end transcriptional signals. The ability of the
CC polymerase to override the gene end signals as it is producing the
CC antigenome is probably due to replicative RNA becoming encapsidated
CC with nucleoprotein as it is synthesized (By similarity).
CC {ECO:0000250|UniProtKB:P03523, ECO:0000250|UniProtKB:P28887}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- SUBUNIT: Interacts with the P protein; the association of P and L forms
CC the polymerase complex. {ECO:0000250|UniProtKB:Q98776}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged
CC asymmetrically towards the blunt end of the virus.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SIMILARITY: Belongs to the rhabdoviridae protein L family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M20166; AAA48440.1; -; Genomic_RNA.
DR PIR; A28602; ZLVNNJ.
DR SMR; P13615; -.
DR PRIDE; P13615; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR InterPro; IPR017234; RNA-dir_pol_rhabdovirus.
DR Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 3: Inferred from homology;
KW ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion; Zinc.
FT CHAIN 1..2109
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000222845"
FT DOMAIN 598..784
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1640..1837
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT ACT_SITE 1227
FT /note="Nucleophile; for GDP polyribonucleotidyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1651
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1762
FT /note="For mRNA (guanine-N(7)-)-methyltransferase and mRNA
FT (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1795
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT ACT_SITE 1833
FT /note="For mRNA (nucleoside-2'-O-)-methyltransferase 2"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P28887"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA-directed RNA polymerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P28887"
FT BINDING 1081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P03523"
FT BINDING 1667..1676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2109 AA; 241583 MW; 52FF2182953E9F79 CRC64;
MDFNLIEDST HWEEEESDFL LRDILSKEDQ MSYLNSADYN LNSPLISDDM VYLIKRMNHE
EVPPIWRSKE WDSPLDMLKG CQAQPLSHQD MHNWFGTWIQ NIQHDSAQGF TFLKEVDKEA
EMTYDLVSTF LKGWVGKEYP FKPKGREIDS IALVGPLCQK FLDLHKVTLI LNAVSLGETK
ELLTTFKGKY RMSCENIPIA RLRLPSLGPV FMCKGWTYIH KERVLMDRNF LLMCKDVIIG
RMQTFLSMIG RSDNKFSPDQ IYTLANVYRI GDRILEQCGN RAYDLIKMIE PICNLKMMEL
ARLHRPKIPK FPHFEEHLKG SVRELTKKSN KIQALYDLIM SIKDVDLVLV VYGSFRHWGH
PFIDYFEGLK KLYTQVNMEK NIDKEHPQQL ASDLARLVLL KQFSESKKWF VDLSKMPPKH
PFYEHVVNKT WPTAAKIQDF GDNWHKLPLT QCFEIPDLID PSVIYSDKSH SMNKKEVIQH
VRTKPNIPIP SKKELQTMLT NKATNWKVFL KDIDGNGLDD DDLIIGLKGK ERELKIAGRF
FSLMSWRLRE YFVITEYLIK TYYVPLFKGL TMADDLTSVI KKMMDSSSGQ GLDDYSSVCL
ANHIDYEQWN NHQRKESNGP IFRVMGQFLG YPSLIERIHE FFEKSLIYYN GLPDLLTIRN
GTLCNSTKHR VCWNGQKGGL EGLRQKGWSI VNLLVIQREA KIRNTAVKVL AQGDNQVICT
QYKTRKTRSE LELRAVLHQM AGNNNKIMEE IKRGTEKLGL IINDDETMQS ADYLNYGKIP
IFRGVIRGLE TKRWSRVTCV TNDQIPTCAN LMSSVSTNAL TVAHFAESPI NAMIQYNYFG
TFARLLLFMH DPAIRQSLYT VKEKIPGLHT RTFKYAVLYL DPSIGGECGM ALSRFLIRAF
PDPETESLSF WKFIYEHARS LHLKKMAVMF GDLPIAKFRI EHINKLLEDP TSLNISMGMS
PANLLKSEVK KCLIESRSSI KNEIIKDATI YMHQEEEKLR GFLWSINPLF PRFLSEFKAG
TFLGVSEALI NLFQNSRTIR NSFKRRYHKD LDELIIKSEI SSLSHLGSMH YRLGDNHIWS
CSASRADVLR YKSWTRKVVG TTVPHPLEMH GSPSKKENPC QLCNSSGLTY ISVHCPKGIT
DVFNRRGPLP AYLGSNTSES TSILQPWEKE SKIPIIKRAT RLRDAISWFI PPESPLSTCI
LNNIRALTGE DWSSKQHGFK RTGSALHRFS TSRMSNGGFA SQSPATLTRM IATTDTMRDF
GTKNYDFMFQ ASLLYGQMTT SISRYGSPGS CTDHYHIRCK GCIREIEEVE LNTSLEYRTP
VVYHILEKWR NNTGSWGHQI KQLKPAEGNW ESLSPVEQSY QVARCIGFLY GELTHKKSRQ
ADDSSLFPLS IQLKVRGRGF LQGLLDGLMR SSCCQVIHRR SVSTLKRPAN AVYGGLIYLI
DKLSASSPFL SLVRTGPIRQ ELEQVPHKMS TSYPTNIRDL GSIVRNYFKY QCRPVERGHY
KTYYNQIWLF SDVLSTEFIG PMRISSSLLK LLYRSSLTKK DKEELRELAA LSSNLRSGED
WDDLHIKFFS NDLLFCPAEI RHACKFGIQK ENEDIALYPN WGIEYIGNVI DIPVFYRAQN
VQKDIRIPLR IQNPLMSGLR LGQLPTGAHY KMRTIISRLK IPYHDFLACG DGSGGMTVAL
LRLNRASRGI FNSLLDLSDT MLRGSSPEPP SALETLGGER SRCVNGDSCW EHPSDLSDKN
TWKYFLHVKK GCGMSINLIT MDMEVKDPTM SYKIELLVRQ YVPVLLESDC CLIYKTYGTY
IATQKDNSLT LIGSLFHSVQ LVQTDLSSSN TSELYLVCRR LKDYIDTPFV DWIELYDSWE
NQYAFKDIKD EFHRARSLKP ETTLVGIPPQ FIPDPGVNLE TLFQIAGVPT GVAHGVIITS
MQSKNKLISN AIGSMCVISH FVMNTIRTTD SMPGPPSDGD VNKMCSALIG TCFWLSWMES
DLNLYKTCLR SIMKSMPVRW FRALKNGKWF QKWDCKGDAI PKDSRLGDSM ANIGNWIRAW
ELIRDGNISE PFDAAAVEML TTSVDKSLSW KKILKTTGIP RLLNSDTDVI DQSILNVQID
IVENQAWQN
